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Related Concept Videos

Complement System01:27

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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A complementation test is a simple cross to identify whether the two mutations are located on the same gene or different genes. It was first performed by Edward Lewis in the 1940s while working on fruit flies. He developed the test to identify the location and arrangement of different mutations on chromosomes.
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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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Transcription activators are proteins that promote the transcription of genes from DNA to RNA. In most cases, these proteins contain two separate domains ‒ a domain that binds to DNA and a domain for activating transcription; however, in some cases, a single domain is responsible for both binding and activation of transcription, as seen in the glucocorticoid receptor and MyoD.
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Gold Nanoparticle Synthesis
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Complement Activation by PEGylated Gold Nanoparticles.

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    Summary
    This summary is machine-generated.

    Gold nanoparticles (AuNPs) activate the complement system, a key part of innate immunity. While PEGylation reduces this effect, complement activation by PEGylated AuNPs is independent of size or PEG molecular weight.

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    Area of Science:

    • Nanomedicine
    • Immunology
    • Biocompatibility

    Background:

    • Gold nanoparticles (AuNPs) are extensively utilized in biomedical fields.
    • Their immunological properties, especially interactions with the complement system, remain less understood.
    • The complement system is crucial for innate immunity and serves as a biocompatibility indicator.

    Purpose of the Study:

    • To investigate the immunological properties of gold nanoparticles (AuNPs).
    • To explore the interaction between different-sized and polyethylene glycol (PEG)-passivated AuNPs with the complement system.
    • To assess the influence of AuNP size, PEGylation, and molecular weight on complement activation and cellular uptake.

    Main Methods:

    • Utilized a series of AuNPs with varying sizes (10–80 nm) and PEGylation (1–10 kDa).
    • Assessed complement system activation by measuring the formation of SC5b-9 in human serum.
    • Investigated cellular uptake of AuNPs by U937 cells expressing complement receptors.

    Main Results:

    • Citrate-capped AuNPs induced size-dependent complement activation.
    • PEGylation of AuNPs reduced complement activation but did not eliminate it.
    • Complement activation by PEGylated AuNPs was independent of AuNP core size and PEG molecular weight.
    • Cellular uptake of both citrate-capped and PEGylated AuNPs correlated with complement activation levels.

    Conclusions:

    • Gold nanoparticles can activate the innate complement system.
    • PEGylation mitigates but does not fully abolish complement activation by AuNPs.
    • These findings offer new insights into the biocompatibility of PEGylated AuNPs, challenging their perception as inert nanomaterials.